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InterPro: IPR002701 Chorismate mutase

Protein matches Help

UniProtKB

Matches:

2198 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR002701 Chorismate_mutase

Secondary

IPR008951

Type

Domain

Signatures Help

Database	ID	Name	Proteins
PROSITE profile	PS51168	CHORISMATE_MUT_2	2191
SMART	SM00830	CM_2	2181
Signatures in BioMart

InterPro Relationships Help

Parent

IPR020822 Chorismate mutase, type II

Children

IPR010950 Chorismate mutase, archaeal
IPR010952 Chorismate mutase, gammaproteobacteria
IPR010954 Chorismate mutase, Gram-positive bacteria/Deinococcus
IPR010957 Gamma/beta/epsilon proteobacterial P-protein, chorismate mutase domain
IPR010958 Chorismate mutase, high GC Gram-positive bacteria/archaeal
IPR011277 Chorismate mutase, T-protein
IPR011279 Chorismate mutase, Gram-positive

Found in

IPR008240 Chorismate mutase, periplasmic
IPR008241 Isochorismate pyruvate-lyase, salicylic acid biosynthesis
IPR010951 Chorismate mutase, bacteria
IPR012044 Chorismate mutase, nematode type

GO Term annotation Help

Process

GO:0046417 chorismate metabolic process

InterPro annotation

Entry Details in BioMart

Abstract

Chorismate mutase, EC:5.4.99.5, catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine [1, 2]. Prephenate dehydratase (IPR001086, EC:4.2.1.51, PDT) catalyses the decarboxylation of prephenate into phenylpyruvate. In microorganisms PDT is involved in the terminal pathway of the biosynthesis of phenylalanine. In some bacteria, such as Escherichia coli, PDT is part of a bifunctional enzyme (P-protein) that also catalyzes the transformation of chorismate into prephenate (chorismate mutase) while in other bacteria it is a monofunctional enzyme. The sequence of monofunctional chorismate mutase aligns well with the N-terminal part of P-proteins [1].

Structural links Help

PDB - click here

SCOP: a.130.1.1 , a.130.1.3 , a.130.1.4

CATH: 1.20.59.10

Database links Help

PROSITE doc: PDOC51167

PANDIT: PF01817

Blocks: IPB002701

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002701

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0A9J8 P-protein

Q57696 Uncharacterized protein MJ0246

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR010952	Chorismate mutase, gammaproteobacteria
IPR010950	Chorismate mutase, archaeal
IPR001086	Prephenate dehydratase
IPR008242	Bifunctional P-protein, chorismate mutase/prephenate dehydratase
IPR018528	Prephenate dehydratase, conserved site
IPR002701	Chorismate mutase
IPR020822	Chorismate mutase, type II
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Schnappauf G, Krappmann S, Braus GH. Tyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutase. J. Biol. Chem. 273 17012-7 1998 [PubMed: 9642265] http://dx.doi.org/10.1074/jbc.273.27.17012
2.	Zhang S, Pohnert G, Kongsaeree P, Wilson DB, Clardy J, Ganem B. Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins. J. Biol. Chem. 273 6248-53 1998 [PubMed: 9497350] http://dx.doi.org/10.1074/jbc.273.11.6248

Additional Reading Open in usermanual
	Kim SK, Reddy SK, Nelson BC, Vasquez GB, Davis A, Howard AJ, Patterson S, Gilliland GL, Ladner JE, Reddy PT. Biochemical and structural characterization of the secreted chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ enzyme not regulated by the aromatic amino acids. J. Bacteriol. 188 2006 8638-48 [PubMed: 17146044] http://dx.doi.org/10.1128/JB.00441-06
	Strater N, Schnappauf G, Braus G, Lipscomb WN. Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures. Structure 5 1997 1437-52 [PubMed: 9384560] http://dx.doi.org/10.1016/S0969-2126(97)00294-3
	Okvist M, Dey R, Sasso S, Grahn E, Kast P, Krengel U. 1.6 A crystal structure of the secreted chorismate mutase from Mycobacterium tuberculosis: novel fold topology revealed. J. Mol. Biol. 357 2006 1483-99 [PubMed: 16499927] http://dx.doi.org/10.1016/j.jmb.2006.01.069
	MacBeath G, Kast P, Hilvert D. A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii. Biochemistry 37 1998 10062-73 [PubMed: 9665711] http://dx.doi.org/10.1021/bi980449t
	Pervushin K, Vamvaca K, Vogeli B, Hilvert D. Structure and dynamics of a molten globular enzyme. Nat. Struct. Mol. Biol. 14 2007 1202-6 [PubMed: 17994104] http://dx.doi.org/10.1038/nsmb1325
	Zaitseva J, Lu J, Olechoski KL, Lamb AL. Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa. J. Biol. Chem. 281 2006 33441-9 [PubMed: 16914555] http://dx.doi.org/10.1074/jbc.M605470200
	Chook YM, Ke H, Lipscomb WN. Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog. Proc. Natl. Acad. Sci. U.S.A. 90 1993 8600-3 [PubMed: 8378335] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=8378335
	Xia T, Song J, Zhao G, Aldrich H, Jensen RA. The aroQ-encoded monofunctional chorismate mutase (CM-F) protein is a periplasmic enzyme in Erwinia herbicola. J. Bacteriol. 175 1993 4729-37 [PubMed: 8335631] http://jb.asm.org/cgi/content/abstract/175/15/4729
	Helmstaedt K, Krappmann S, Braus GH. Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase. Microbiol. Mol. Biol. Rev. 65 2001 404-21, table of contents [PubMed: 11528003] http://dx.doi.org/10.1128/MMBR.65.3.404-421.2001
	Qamra R, Prakash P, Aruna B, Hasnain SE, Mande SC. The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions. Biochemistry 45 2006 6997-7005 [PubMed: 16752890] http://dx.doi.org/10.1021/bi0606445

InterPro 23.1